1W8H

structure of pseudomonas aeruginosa lectin II (PA-IIL)complexed with lewisA trisaccharide

Summary for 1W8H

• Entry DOI: 10.2210/pdb1w8h/pdb
• Related: 1GZT 1OUR 1OUS 1OUX 1OVP 1OVS 1OXC 1UZV 1W38 1W43 1W8F
• Descriptor: PSEUDOMONAS AERUGINOSA LECTIN II, alpha-L-fucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-galactopyranose-(1-3)-[alpha-L-fucopyranose-(1-4)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: sugar binding protein, lectin, sugar, lewis a, cystic fibrosis
• Biological source: PSEUDOMONAS AERUGINOSA
• Total number of polymer chains: 4
• Total formula weight: 50573.80

Authors

Perret, S.,Sabin, C.,Dumon, C.,Budova, M.,Gautier, C.,Galanina, O.,Ilia, S.,Bovin, N.,Nicaise, M.,Desmadril, M.,Gilboa-Garber, N.,Wimmerova, M.,Mitchell, E.P.,Imberty, A. (deposition date: 2004-09-21, release date: 2005-03-31, Last modification date: 2024-02-14)

Primary citation

Perret, S.,Sabin, C.,Dumon, C.,Pokorna, M.,Gautier, C.,Galanina, O.,Ilia, S.,Bovin, N.,Nicaise, M.,Desmadril, M.,Gilboa-Garber, N.,Wimmerova, M.,Mitchell, E.P.,Imberty, A.
Structural Basis for the Interaction between Human Milk Oligosaccharides and the Bacterial Lectin Pa-Iil of Pseudomonas Aeruginosa.
Biochem.J., 389:325-, 2005

PubMed Abstract: One of the mechanisms contributing to the protection by breast-feeding of the newborn against enteric diseases is related to the ability of human milk oligosaccharides to prevent the attachment of pathogenic bacteria to the duodenual epithelium. Indeed, a variety of fucosylated oligosaccharides, specific to human milk, form part of the innate immune system. In the present study, we demonstrate the specific blocking of PA-IIL, a fucose-binding lectin of the human pathogen Pseudomonas aeruginosa, by milk oligosaccharides. Two fucosylated epitopes, Lewis a and 3-fucosyl-lactose (Lewis x glucose analogue) bind to the lectin with dissociation constants of 2.2x10(-7) M and 3.6x10(-7) M respectively. Thermodynamic studies indicate that these interactions are dominated by enthalpy. The entropy contribution is slightly favourable when binding to fucose and to the highest-affinity ligand, Lewis a. The high-resolution X-ray structures of two complexes of PA-IIL with milk oligosaccharides allow the precise determination of the conformation of a trisaccharide and a pentasaccharide. The different types of interaction between the oligosaccharides and the protein involve not only hydrogen bonding, but also calcium- and water-bridged contacts, allowing a rationalization of the thermodynamic data. This study provides important structural information about compounds that could be of general application in new therapeutic strategies against bacterial infections.

PubMed: 15790314
DOI: 10.1042/BJ20050079

Experimental method

X-RAY DIFFRACTION (1.75 Å)